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FILE 'CAPLUS, MEDLINE , BIOSIS, EMBASE ' ENTERED AT 13:02:57 ON 31 MAR 2004

T 1

T A G A

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b J lANG . IN .

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b LI AND FUblON PROTEIN

DUP KhM Lz (b DUPLICATES REMOVED;

b EAPREbffffff bAME FUSION PROTEIN SAME REPOTER SAME LIBRARffffff

S EXPRESffffff ( 10A) FUSION PROTEIN (10A) REPORTERff

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b Lll AND SCREENffffff

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DUP REM LI J (1 DUPL1L.A1L REMOVED;

L17

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S LI. IN.

L18

153

S LI 7 AND CYCLOHEXIMIDE

L19

S L18 AND FLUORESCENT PROTEIN

L20

S LI 8 AND FUSION PROTEIN

L21

S L17 AND FLUORESCENT PROTEIN

L22

S L21 AND LIBRAR###

L23

S L21 AND SCREEN###

FILE 'CAPLUS' ENTERED AT 13:02:57 ON 31 MAR 2004

USE IS SUBJECT TO THE TERMS OF YOUR STN CUSTOMER AGREEMENT.

PLEASE SEE "HELP USAGETERMS " FOR DETAILS.

FILE 1 MEDLINE 1 ENTERED AT 13:02:57 ON 31 MAR 2 004

FILE MIOSIS' ENTERED AT 13:02:57 ON 31 MAR 2 0 04
COPYRIGHT (C) 2 004 BIOLOGICAL ABSTRACTS INC. (R)

FILE 'EMBASE 1 ENTERED AT 13:02:57 ON 31 MAR 2004
COPYRIGHT (C) 2 004 Elsevier Inc. All rights reserved.

=> s Jiang. in.

LI 1090 JIANG. IN.

=> s 11 and fusion protein

L2 8 LI AND FUSION PROTEIN

=> dup rem 112

L12 IS NOT VALID HERE

The L-number entered has not been defined in this session, or it
has been deleted. To see the L-numbers currently defined in this
session, enter DISPLAY HISTORY at an arrow prompt ( = >) .

=> dup rem 12

PROCESSING COMPLETED FOR L2

L3 2 DUP REM L2 (6 DUPLICATES REMOVED)

=> d 13 1-2 bib ab kwic

L3 ANSWER 1 OF 2 CAPLUS COPYRIGHT 2 004 ACS on STN DUPLICATE 1
AN 1999:320171 CAPLUS
DN 131:100245

TI Expression of a truncated receptor protein tyrosine phosphatase kappa in

the brain of an adult transgenic mouse
AU Shen, P.; Canoll, P. D.; Sap, J.; Musacchio, J. M.

CS Department of Pharmacology, New York University Medical Center, New York,

NY, 10016, USA
SO Brain Research (1999), 826(2), 157-171

CODEN: BRREAP; ISSN: 0006-8993
PB Elsevier Science B.V.
DT Journal
LA English

AB Receptor protein tyrosine phosphatases (RPTPs) comprise a family of

proteins that feature intracellular phosphatase domains and an ectodomain
with putative ligand-binding motifs'. Several RPTPs are expressed in the
brain, including RPTP-K which participates in homophilic cell-cell
interactions in vitro (Jiang, Y.-P et al . , 1993; Sap, J. et al . ,
1994). The homol. of RPTP-k's ectodomain to neural cell adhesion
mols. indicates potential roles in developmental processes such as axonal
growth and target recognition, as has been demonstrated for certain
Drosophila RPTPs. The brain distribution of RPTP-K-expressing cells
has not been determined, however. In a gene-trap mouse model with a P-gal
+ neo (1-geo) insertion in the endogenous RPTP-k gene, the
consequent loss of RPTP-k's enzymic activity does not produce any
obvious phenotypic defects (Skarnes, W. C. et al . , 1995). Nevertheless,
since the transgene • s expression is driven by the endogenous RPTP-k
promoter, distribution of the truncated RPTP-K/p-geo
fusion protein should reflect the regional and cellular
expression of wild-type RPTP-k, and thus may identify sites where
RPTP-k is important. Towards that goal, the authors have used this
mouse model to map the distribution of the truncated RPTP-K/p-
geo fusion protein in the adult mouse brain using

p-galactosidase as a marker enzyme. Visualization of the
p-galactosidase activity revealed a non-random pattern of expression,
and identified cells throughout the CNS that display RPTP-k promoter
activity. Several neural systems highly expressed the transgene-most
notably cortical, olfactory, hippocampal, hypothalamic, amygdaloid and
visual structures. These well -characterized brain regions may provide a
basis for future studies of RPTP-k function.
RE.CNT 4 0 THERE ARE 4 0 CITED REFERENCES AVAILABLE FOR THIS RECORD

ALL CITATIONS AVAILABLE IN THE RE FORMAT
AB Receptor protein tyrosine phosphatases (RPTPs) comprise a family of

proteins that feature intracellular phosphatase domains and an ectodomain
with putative ligand-binding motifs. Several RPTPs are expressed in the
brain, including RPTP-K which participates in homophilic cell-cell
interactions in vitro (Jiang, Y.-P et al . , 1993; Sap, J. et al . ,
1994). The homol . of RPTP-k' s ectodomain to neural cell adhesion
mols. indicates potential roles in developmental processes such as axonal
growth and target recognition, as has been demonstrated for certain
Drosophila RPTPs. The brain distribution of RPTP-K-expressing cells
has not been determined, however. In a gene -trap mouse model with a p-gal
+ neo (1-geo) insertion in the endogenous RPTP-k gene, the
consequent loss of RPTP-k's enzymic activity does not produce any
obvious phenotypic defects (Skarnes, W. C. et al . , 1995). Nevertheless,
since the transgene ' s expression is driven by the endogenous RPTP-k
promoter, distribution of the truncated RPTP-K/p-geo
fusion protein should reflect the regional and cellular
expression of wild-type RPTP-k, and thus may identify sites where
RPTP-k is important. Towards that goal, the authors have used this
mouse model to map the distribution of the truncated RPTP-k/P-
geo fusion protein in the adult mouse brain using
p-galactosidase as a marker enzyme. Visualization of the
p-galactosidase activity revealed a non-random pattern of expression,
and identified cells throughout the CNS that display RPTP-k promoter
activity. Several neural systems highly expressed the transgene-most
notably cortical, olfactory, hippocampal, hypothalamic, amygdaloid and
visual structures. These well-characterized brain regions may provide a
basis for future studies of RPTP-k function.

ANSWER 2 OF 2 CAPLUS COPYRIGHT 2 004 ACS on STN DUPLICATE 2
1997:698880 CAPLUS
128 :31575

Cloning and expression of a gene encoding a protein obtained from
earthworm secretion that is a chemoattractant for garter snakes
Liu, Weimin; Wang, Dalton; Chen, Ping; Halpern, Mimi

Department of Biochemistry, SUNY Health Science Center at Brooklyn, NY,
11203, USA

Journal of Biological Chemistry (1997), 272(43), 27378-27381
CODEN: JBCHA3; ISSN: 0021-9258

American Society for Biochemistry and Molecular Biology
Journal
English

The protein ES20, derived from earthworm shock secretion, is a
vomeronasally mediated chemoattractant for garter snakes (Jiang,
X. C, Inouchi, J., Wang, D., and Halpern, M. (1990) J. Biol. Chemical 265,
8736-8744) . Based on its 15-residue N-terminal amino acid sequence,
degenerative oligodeoxynucleotide probes were synthesized and used to
screen a cDNA library that was constructed in sense orientation using a
Uni-ZAP XR vector and XLl-Blue MRF 1 host. A gene was cloned from a
polymerase chain reaction as well as from the cDNA library. A combination
of the forward degenerative primer and T7 primer was used to obtain
gene-specific DNA fragments, from which probes were synthesized and
successfully used in screening the cDNA library. The ES2 0 gene is about
700 base pairs long and encodes 208 amino residues. The ES20 gene was
excised from a recombinant plasmid pSK-ES20, ligated to pQE30 expression
vector, and transformed into Escherichia coli strain JM109. The selected

L3
AN
DN
TI

AU
CS

PB
DT
LA
AB

recombinant plasmids were transformed into expression host cell, E. coli
M15 [pREP4] . Three transf ormants were selected, induced with
isopropyl-l-thio-p-D-galactopyranoside for fusion gene expression and
an expressed 20-kDa fusion protein purified under

denaturing conditions. This protein was refolded and gave a pos . reaction
against ES20-specif ic polyclonal antibodies. The fusion
protein that had not been denatured remained as an aggregate and
was an active chemoattractant for garter snakes.

RE.CNT 19 THERE ARE 19 CITED REFERENCES AVAILABLE FOR THIS RECORD
ALL CITATIONS AVAILABLE IN THE RE FORMAT

AB The protein ES2 0, derived from earthworm shock secretion, is a

vomeronasally mediated chemoattractant for garter snakes (Jiang,
X. C, Inouchi, J. , Wang, D., and Halpern, M. (1990) J. Biol. Chemical 265,
8736-8744) . Based on its 15-residue N-terminal amino acid sequence,
degenerative oligodeoxynucleotide probes were synthesized and used to
screen a cDNA library that was constructed in sense orientation using a
Uni-ZAP XR vector and XLl-Blue MRF 1 host. A gene was cloned from a
polymerase chain reaction as well as from the cDNA library. A combination
of the forward degenerative primer and T7 primer was used to obtain
gene-specific DNA fragments, from which probes were synthesized and
successfully used in screening the cDNA library. The ES20 gene is about
700 base pairs long and encodes 2 08 amino residues. The ES2 0 gene was
excised from a recombinant plasmid pSK-ES20, ligated to pQE30 expression
vector, and transformed into Escherichia coli strain JM109. The selected
recombinant plasmids were transformed into expression host cell, E. coli
M15 [pREP4] . Three transf ormants were selected, induced with
isopropyl-l-thio-p-D-galactopyranoside for fusion gene expression and
an expressed 20-kDa fusion protein purified under

denaturing conditions. This protein was refolded and gave a pos. reaction
against ES20-specif ic polyclonal antibodies. The fusion
protein that had not been denatured remained as an aggregate and
was an active chemoattractant for garter snakes.

=> s expres### same fusion protein same repoter same librar###

L4 0 EXPRES### SAME FUSION PROTEIN SAME REPOTER SAME LIBRAR###

=> s expres### (10a) fusion protein (10a) reporter#

L5 35 EXPRES###(10A) FUSION PROTEIN (10A) REPORTER#

=> s 15 and librar###

L6 4 L5 AND LIBRAR###

=> s 16 and cycloheximide

L7 0 L6 AND CYCLOHEXIMIDE

=> dup rem 16

PROCESSING COMPLETED FOR L6

L8 4 DUP REM L6 (0 DUPLICATES REMOVED)

=> d 18 1-4 bib ab kwic

L8 ANSWER 1 OF 4 CAPLUS COPYRIGHT 2 004 ACS on STN
AN 2003:656310 CAPLUS
DN 139:174827

TI Methods and kits for isolating and characterizing short-lived proteins and

arrays derived therefrom for use in drug screening
IN Li, Xianqiang; Jiang, Xin
PA USA

SO U.S. Pat. Appl. Publ., 30 pp., Cont . -in-part of U.S. Ser. No. 53,230.

CODEN: USXXCO
DT Patent
LA English
FAN.CNT 3

PATENT NO. KIND DATE APPLICATION NO. DATE

2003157540

20030821

2003

-347160

20030116

2003134287

20030717

2002

-53230

20020116

2003134288

20030717

2002

-53516

20020116

PRAI

2002-53230

20020116

2002-53516

20020116

AB Compns . , kits and methods are provided for isolating and characterizing
short-lived proteins. The method comprises taking a library of
cells wherein each cell in the library expresses a
fusion protein comprising a reporter protein

and a protein encoded by a sequence from a cDNA library derived
from a sample of cells.. The sequence from the cDNA library is
varied within the cell library and the rate of protein
expression or degradation by cells in the library is modified. A
population of cells is selected from the library of cells based
on the population of cells having different reporter signal intensities
than other cells in the library wherein the difference between
intensities is indicative of the population of cells expressing shorter
lived fusion proteins than the fusion proteins expressed by the other
cells in the library and determining protein sequences of the fusion
proteins of the selected population of cells. Also provided are
oligonucleotide, protein and antibody arrays derived from short-lived
proteins. The arrays can be used for efficiently profiling expression of
short-lived proteins, screening for binding agents and comparing
expression levels under different conditions.
AB Compns., kits and methods are provided for isolating and characterizing
short-lived proteins. The method comprises taking a library of
cells wherein each cell in the library expresses a
fusion protein comprising a reporter protein

(library; methods and kits for isolating and characterizing
short-lived proteins and arrays derived therefrom for use in drug
screening)
IT cDNA library

(proteins encoded by; methods and kits for isolating and characterizing
short-lived proteins and arrays derived therefrom for use in drug
screening)

L8 ANSWER 2 OF 4 CAPLUS COPYRIGHT 2 004 ACS on STN
AN 2002:353656 CAPLUS
DN 136:351377

TI Screening genes encoding nuclear transport proteins by GFP fusion protein

expression and cell sorting
IN Maekawa, Takami; Mori, Maiko; Takahara, Yoshiyuki
PA Aj inomoto Co . , Inc . , Japan
SO PCT Int. Appl., 60 pp.

CODEN: PIXXD2
DT Patent

LA Japanese
FAN.CNT 1

PATENT NO.

KIND DATE

APPLICATION NO. DATE

PI WO 2002036823 Al 20020510 WO 2001-JP9700 20011106

W: AE, AG, AL, AM, AT, AU, AZ , BA, BB, BG, BR, BY, BZ, CA, CH, CN,
CO, CR, CU, CZ, DE, DK, DM, DZ, EC, EE, ES , PI, GB, GD, GE, GH,
GM, HR, HU, ID, IL, IN, IS, JP, KE, KG, KP, KR, KZ, LC, LK, LR,
LS, LT, LU, LV, MA, MD, MG, MK, MN, MW, MX, MZ, NO, NZ, OM, PH,
PL, PT, RO, RU, SD, SE, SG, SI, SK, SL, TJ, TM, TR, TT, TZ, UA,
UG, US, UZ, VN, YU, ZA, ZW, AM, AZ, BY, KG, KZ, MD, RU, TJ, TM
RW: GH, GM, KE, LS, MW, MZ , SD, SL, SZ, TZ , UG, ZW, AT, BE, CH, CY,
DE, DK, ES, FI, FR, GB, GR, IE, IT, LU, MC, NL, PT, SE, TR, BF,
BJ, CF, CG, CI, CM, GA, GN, GQ, GW, ML, MR, NE, SN, TD, TG
AU 2002011021 A5 20020515 AU 2002-11021 20011106

EP 1333099 Al 20030806 EP 2001-979034 20011106

R: AT, BE, CH, DE, DK, ES, FR, GB, GR, IT, LI, LU, NL, SE, MC , PT,
IE, SI, LT, LV, FI, RO, MK, CY, AL, TR
US 2003180801 Al 20030925 US 2002-204310 20020821

PRAI JP 2000-337906 A 20001106
WO 2001-JP9700 W 20011106
AB A method for screening a gene encoding a protein specifically transporting

into nucleus by cloning each gene in a group of a large number of genes into
an expression vector to express as fusion
protein with a marker or reporter protein to construct a
gene expression library, introducing this gene expression
library into two cell groups to express the fusion proteins,
stimulating one of the cell groups, separating cells wherein the fusion
proteins are localized in the nucleus of such cells from both cell groups,
and comparing the separated cells or nuclei to thereby search for a gene
encoding a protein specifically transporting into the nucleus upon
stimulus, is disclosed. A nuclear localization signal is used in fusion
protein. Cell sorting, flow cytometry, microdissection, or microscopy
observation, is used to sort cells. 11 ESTs and 6 unknown genes coding
for proteins transporting into nucleus were identified by expressing as
GFP fusion proteins in HepG2 cells and stimulating with TNFa . Eight
unknown genes were also identified by heat shock stimulation.
RE.CNT 1 THERE ARE 1 CITED REFERENCES AVAILABLE FOR THIS RECORD

ALL CITATIONS AVAILABLE IN THE RE FORMAT
AB A method for screening a gene encoding a protein specifically transporting

into nucleus by cloning each gene in a group of a large number of genes into
an expression vector to express as fusion
protein with a marker or reporter protein to construct a
gene expression library, introducing this gene expression
library into two cell groups to express the fusion proteins,
stimulating one of the cell groups, separating cells wherein the fusion
proteins are localized in the nucleus of such cells from both cell groups,
and comparing the separated cells or nuclei to thereby search for a gene
encoding a protein specifically transporting into the nucleus upon
stimulus, is disclosed. A nuclear localization signal is used in fusion
protein. Cell sorting, flow cytometry, microdissection, or microscopy
observation, is used to sort cells. 11 ESTs and 6 unknown genes coding
for proteins transporting into nucleus were identified by expressing as
GFP fusion proteins in HepG2 cells and stimulating with TNFa. Eight
unknown genes were also identified by heat shock stimulation.
IT Nucleic acid library

(gene expression; screening genes encoding nuclear transport proteins
by GFP fusion protein expression and cell sorting)

L8 ANSWER 3 OF 4 CAPLUS COPYRIGHT 2 004 ACS on STN
AN 1997:740333 CAPLUS
DN 128:10873

TI A three -hybrid reporter gene method for screening for proteins binding
defined ligands

IN Liu, Jun; Licitra, Edward J.

PA Massachusetts Institute of Technology, USA

SO PCT Int. Appl., 4 0 pp.

COD EN: PIXXD2
DT Patent
LA English
FAN.CNT 1

PATENT NO. KIND DATE APPLICATION NO. DATE

PI wo

9741255
W: CA,

iyy / hod

1 Q07A/1TC

iyy /U4^b

RW: AT,

BE,

nrr TM7*

CH, Dh ,

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2252886

1 Q Q *7 1 1 C\d

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907750

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iyy /U4zb

907750

2 002 0918

R: AT,

BE,

CH, DE,

DK, ES,

FR,

GB, GR, IT, LI, LU,

NL, SE,

IE,

5928868

19990727

US 1997-845674

19970425

2000508923

20000718

JP 1997-539036

19970425

29724617

20020718

DE 1997-29724617

19970425

1241265

20020918

EP 2002-76267

19970425

1241265

20040218

R: AT,

BE,

CH, DE,

DK, ES,

FR,

GB, GR, IT, LI, LU,

NL, SE,

IE,

SI,

LT, LV,

FI, RO,

MK,

CY, AL

224454

20021015

AT 1997-921370

19970425

2183166

20030316

ES 1997-921370

19970425

PRAI US

1996-17341P

19960426

1997-921370

19970425

1997-US6912

19970425

NL, PT, SE

MC, PT,

AB A method for identifying the binding partner for a define ligand using an
extension of the two-hybrid system is described. The method uses a fusion
protein of the LexA protein and a ligand binding protein to bind to a LexA
operator upstream of a reporter gene. This is bound to by a conjugate of
the natural ligand for the protein and the ligand of interest. Possible
binding partners for the ligand are identified by introduction of an
expression library in which the proteins are synthesized as
fusion products with a transcriptional activator. When the necessary
combination of LexA fusion protein, ligand, and transcriptional activator
fusion protein are brought together, the
reporter gene is expressed. The method is particularly
intended for the identification of natural binding partners for small
mols. A fusion product of LexA and the rat glucocorticoid receptor is
used in a reconstruction experiment with FK506-binding protein FKBP12 is used
to demonstrate using a conjugate of dexamethasone and FK506 as the hybrid
ligand .

IT Combinatorial library

(nucleic acid, screening for ligand-binding proteins of; three-hybrid
reporter gene method for screening for proteins binding defined

ligands)
IT Nucleic acid library

(screening for ligand-binding proteins of; three-hybrid reporter gene
method for screening for proteins binding defined ligands)

L8 ANSWER 4 OF 4 MEDLINE on STN

AN 9714 0325 MEDLINE
DN PubMed ID: 8986806

TI A novel member of the RING finger family, KRIP-1, associates with the
KRAB-A transcriptional repressor domain of zinc finger proteins.

AU Kim S S; Chen Y M; 0 ' Leary E; Witzgall R; Vidal M; Bonventre J V

CS Renal Unit, Massachusetts General Hospital, Charlestown 02129, USA.

NC DK 38452 (NIDDK)
DK 39773 (NIDDK)
NS 10828 (NINDS)

SO Proceedings of the National Academy of Sciences of the United States of

America, (1996 Dec 24) 93 (26) 15299-304.

Journal code: 7505876. ISSN: 0027-8424.
CY United States

DT Journal; Article; (JOURNAL ARTICLE)

LA English

FS Priority Journals

OS GENBANK-U673 03

EM 199701

ED Entered STN: 19970219

Last Updated on STN: 19970219
Entered Medline: 19970128

AB The Kruppel-associated box A (KRAB-A) domain is an evolutionarily

conserved transcriptional repressor domain present in approximately
one-third of zinc finger proteins of the Cys2-His2 type. Using the yeast
two-hybrid system, we report the isolation of a cDNA encoding a novel
murine protein, KRAB-A interacting protein 1 (KRIP-1) that physically
interacts with the KRAB-A region. KRIP-1 is a member of the RBCC
subfamily of the RING finger, or Cys3HisCys4, family of zinc binding
proteins whose other members are known to play important roles in
differentiation, oncogenesis, and signal transduction. The KRIP-1 protein
has high homology to TIF1, a putative modulator of ligand- dependent
activation function of nuclear receptors. A 3.5-kb mRNA for KRIP-1 is
ubiquitously expressed among all adult mouse tissues studied. When a
GAL4 -KRIP-1 fusion protein is expressed in

COS cells with a chloramphenicol acetyltransf erase reporter
construct with five GAL 4 binding sites, there is dose-dependent repression
of transcription. Thus, KRIP-1 interacts with the KRAB-A region of C2H2
zinc finger proteins and may mediate or modulate KRAB-A transcriptional
repressor activity.

AB ... of nuclear receptors. A 3.5-kb mRNA for KRIP-1 is ubiquitously
expressed among all adult mouse tissues studied. When a GAL4 -KRIP-1
fusion protein is expressed in COS cells with

a chloramphenicol acetyltransf erase reporter construct with five
GAL4 binding sites, there is dose-dependent repression of transcription.
Thus, KRIP-1 interacts with the KRAB-A region of.
CT Check Tags : Support, Non-U. S. Gov't; Support, U.S. Gov't, P.H.S.

Amino Acid Sequence

Animals

Base Sequence

COS Cells

Conserved Sequence
Embryo

Gene Library
Kidney: ME, metabolism
Mice

Molecular Sequence Data

Nuclear Proteins: BI, biosynthesis

Nuclear Proteins: CH, chemistry

*Nuclear Proteins: ME, .

=> s fusion (10a) green fluorescence ( 10a) librar###

L9 0 FUSION (10A) GREEN FLUORESCENCE ( 1 OA) LIBRAR###

=> s fusion (10a) green (10a) protein (10a) librar###

L10 40 FUSION (10A) GREEN (10A) PROTEIN (10A) LIBRAR###

=> s 110 and expres###

Lll 15 L10 AND EXPRES###

=> s 111 and cycloheximide

L12 0 Lll AND CYCLOHEXIMIDE

=> 111 and screen###

Lll IS NOT A RECOGNIZED COMMAND

The previous command name entered was not recognized by the system.
For a list of commands available to you in the current file, enter
"HELP COMMANDS" at an arrow prompt (=>) .

=> s 111 and screen###

L13 10 Lll AND SCREEN###

=> s 113 and (inhibit### ( 10a) degradat###)

L14 0 L13 AND ( INHIBIT### ( 10A) DEGRADAT###)

=> s 113 and inhibit###

L15 0 L13 AND INHIBIT###

=> dup rem 113

PROCESSING COMPLETED FOR L13

LI 6 9 DUP REM LI 3 (1 DUPLICATE REMOVED)

=> d 116 1-9 bib ab kwic

L16
AN
DN
TI

IN
PA
SO

DT
LA

ANSWER 1 OF 9 CAPLUS COPYRIGHT 2 0 04 ACS on STN DUPLICATE 1
2003 : 296076 CAPLUS
138 :315791

Fusions of random peptide libraries in scaffold proteins such as green
fluorescent protein or p-lactamase

Anderson, David; Peelle, Beau Robert; Bogenberger, Jakob Maria
Rigel Pharmaceuticals, Inc., USA

U.S., 63 pp. , Cont .
CODEN; USXXAM
Patent
English

-in-part of U.S. 6,180,343.

FAN.CNT 4

PATENT NO.

KIND

DATE

APPLICATION NO.

DATE

6548632

20030415

1999-415765

19991008

6180343

20010130

1998-169015

19981008

6548249

20030415

2000-626581

20000727

6562617

20030513

2000-626580

20000727

2001003650

20010614

2000-749959

20001227

6596485

20030722

2003143562

20030731

2002-177725

20020620

2003224412

20031204

2003-393449

20030318

1998-169015

19981008

1999-415765

19991008

2002-177725

20020620

particularly

The invention relates to the use of scaffold proteins,
green fluorescent protein (GFP) and p-lactamase
TEM-1, in fusion constructs with random and defined peptides and

peptide libraries. The fusions act to increase the cellular
expression levels, decrease the cellular catabolism, increase the
conformational stability relative to linear peptides, and increase the
steady state concns . of the random peptides and random peptide library
members expressed in cells for the purpose of detecting the
presence of the peptides and screening random peptide libraries.
N- terminal, C- terminal, dual N- and C- terminal, and one or more internal
fusions are all contemplated. Internal fusions in Renilla GFP may be made
in loops 1-5 (amino acid residues 130-135, 154-159, 172-175, 188-193, or
208-216) for optimal presentation of the peptide. Inclusion of multiple
highly flexible amino acid residues between GFP and the library allows
minimal conformational constraints on the GFP. Designed insertion sites
in loops 2-4 retain a high level of GFP fluorescence when the inserts are
flanked by multiple glycines in the tetrapeptide linkers. Novel fusions
utilizing self-binding peptides to create a conf ormationally stabilized
fusion domain are also contemplated.

RE.CNT 44 THERE ARE 44 CITED REFERENCES AVAILABLE FOR THIS RECORD

ALL CITATIONS AVAILABLE IN THE RE FORMAT

AB The invention relates to the use of scaffold proteins, particularly
green fluorescent protein (GFP) and p-lactamase

TEM-1, in fusion constructs with random and defined peptides and
peptide libraries. The fusions act to increase the cellular
expression levels, decrease the cellular catabolism, increase the ,
conformational stability relative to linear peptides, and increase the
steady state concns. of the random peptides and random peptide library
members expressed in cells for the purpose of detecting the
presence of the peptides and screening random peptide libraries.
N-terminal, C- terminal, dual N- and C-terminal, and one or more internal
fusions are all contemplated. Internal fusions in Renilla GFP may be made
in loops 1-5 (amino acid residues 130-135, 154-159, 172-175, 188-193, or
208-216) for optimal presentation of the peptide. Inclusion of multiple
highly flexible amino acid residues between GFP and the library allows
minimal conformational constraints on the GFP. Designed insertion sites
in loops 2-4 retain a high level of GFP fluorescence when the inserts are
flanked by multiple glycines in the tetrapeptide linkers. Novel fusions
utilizing self-binding peptides to create a conf ormationally stabilized
fusion domain are also contemplated.
ST scaffold protein fusion random peptide library; green
fluorescent protein fusion random peptide
library; lactamase fusion random peptide library
IT Animal cell line

(293, GFP fusions expressed in; fusions of random peptide
libraries in scaffold proteins such as green fluorescent protein or
p-lactamase)
IT Animal cell line

(JURKAT, GFP fusions expressed in; fusions of random peptide
libraries in scaffold proteins such as green fluorescent protein or
p-lactamase)

L16 ANSWER 2 OF 9 CAPLUS COPYRIGHT 2 004 ACS on STN
AN 2003:950623 CAPLUS
DN 140:13712

TI Structurally biased random peptide libraries based on different scaffolds
IN Anderson, David; Peelle, Beau Robert; Bogenberger, Jakob Maria
PA USA

SO U.S. Pat. Appl. Publ., 110 pp., Cont . -in-part of U.S. Ser. No. 177,725.

CODEN: USXXCO
DT Patent
LA English
FAN.CNT 4

PATENT NO. KIND DATE APPLICATION NO. DATE

PI US 2003224412 Al 20031204

US 6180343 Bl 20010130

US 2003-393449 20030318
US 1998-169015 19981008

US 6548632
US 2003143562

Bl
Al

20030415
20030731

US 1999-415765
US 2002-177725

19991008
20020620

PRAI US 1998-169015 A2 19981008

US 1999-415765 A2 19991008

US 2002-177725 A2 20020620
AB The invention relates to the use of scaffold proteins, particularly

green fluorescent protein (GFP) , in fusion

constructs with random and defined peptides and peptide libraries
, to increase the cellular expression levels, decrease the cellular
catabolism, increase the conformational stability relative to linear
peptides, and to increase the steady state concns . of the library peptides
and peptide library members expressed in cells for the purpose
of detecting the presence of the peptides and screening peptide
libraries. N- terminal, C-terminal, dual N- and C-terminal and one or more
internal fusions are all contemplated. Novel fusions utilizing
self-binding peptides to create a conf ormationally stabilized fusion
domain are also contemplated.
AB The invention relates to the use of scaffold proteins, particularly
green fluorescent protein (GFP) , in fusion

constructs with random and defined peptides and peptide libraries
, to increase the cellular expression levels, decrease the cellular
catabolism, increase the conformational stability relative to linear
peptides, and to increase the steady state concns. of the library peptides
and peptide library members expressed in cells for the purpose
of detecting the presence of the peptides and screening peptide
libraries. N- terminal, C-terminal, dual N- and C-terminal and one or more
internal fusions are all contemplated. Novel fusions utilizing
self-binding peptides to create a conformationally stabilized fusion
domain are also contemplated.
ST scaffold protein fusion random peptide library; green
fluorescent protein fusion random peptide
library; lactamase fusion random peptide library

L16 ANSWER 3 OF 9 CAPLUS COPYRIGHT 2 004 ACS on STN
AN 2003:590695 CAPLUS
DN 139:144918

TI Random peptide libraries in the context of a reporter protein scaffold for

use in analysis of peptide effects on protein structure and function
IN Anderson, David; Peelle, Beau Robert; Bogenberger, Jakob Maria
PA Rigel Pharmaceuticals, Inc., USA

SO U.S. Pat. Appl. Publ., 110 pp., Cont . -in-part of U. S. Ser. No. 415,765.

CODEN: USXXCO
DT Patent
LA English
FAN.CNT 4

PATENT NO.

KIND

DATE

APPLICATION NO.

DATE

2003143562

20030731

US 2002-177725

20020620

6180343

20010130

US 1998-169015

19981008

6548632

20030415

US 1999-415765

19991008

2003224412

20031204

US 2003-393449

20030318

PRAI

1998-169015

19981008

1999-415765

19991008

2002-177725

20020620

AB A method of using a reporter protein as a framework within which the
effects of random peptides from a library on protein structure and
function is described. A DNA library in which the gene for the reporter
protein has sequences encoding random peptides inserted at defined sites
is prepared and expressed in a suitable host. The library may be
biased, e.g. to increase the possibility of including a peptide promoting
an a-helical structure. The peptides may be at the N- terminal, the
C-terminal, or at internal sites. The library is screened for
members showing properties such as increases in cellular reporter

concentration,

increased stability from lower rates of cellular catabolism, increased
conformational stability relative to linear peptides, and increased steady
state concns . of the library peptides. A reporter protein may be replaced
by a protein essential for cell survival. Novel fusions utilizing
self-binding peptides to create a conf ormationally stabilized fusion
domain are also contemplated. Loops in green fluorescent were identified
as potential sites for the peptide library and test peptides. Tests with
two different insertions showed consistent effects on protein fluorescence
in Escherichia coli and mammalian cells.

concentration,

increased stability from lower rates of cellular catabolism, increased
conformational stability relative to linear peptides, and increased steady
state concns. of the library peptides. A reporter protein may be replaced
by a protein essential for cell survival. Novel fusions utilizing
self-binding peptides to create a conf ormationally stabilized fusion
domain are also contemplated. Loops in green fluorescent were identified
as potential sites for the peptide library and test peptides. Tests with
two different insertions showed consistent effects on protein fluorescence
in Escherichia coli and mammalian cells.

ST scaffold protein fusion random peptide library; green
fluorescent protein fusion random peptide
library; lactamase fusion random peptide library

IT Peptides, biological studies

RL: BSU (Biological study, unclassified) ; BIOL (Biological study)
(bioactive, screening for; random peptide libraries in
context of reporter protein scaffold for use in anal, of peptide
effects on protein structure and function)

L16 ANSWER 4 OF 9 BIOSIS COPYRIGHT 2 004 BIOLOGICAL ABSTRACTS INC. on STN
AN 2003:378382 BIOSIS
DN PREV2 003 0 03783 82

TI Green fluorescent protein fusions with random peptides.

AU Anderson, David [Inventor, Reprint Author] ; Bogenberger, Jakob Maria

[Inventor]
CS Menlo Park, CA, USA

ASSIGNEE: Rigel Pharmaceuticals, Inc.
PI US 6596485 July 22, 2003

SO Official Gazette of the United States Patent and Trademark Office Patents,
(July 22 2003) Vol. 1272, No. 4. http://www.uspto.gov/web/menu/patdata.htm
1. e-file..

ISSN: 0098-1133 (ISSN print) .
DT Patent
LA English

ED Entered STN: 13 Aug 2003

Last Updated on STN: 13 Aug 2 003
AB The invention relates to the use of fluorescent proteins, particularly

green fluorescent protein (GFP) , in fusion

Novel fusions utilizing self -binding peptides to create a conf ormationally
stabilized fusion domain are also contemplated.
AB The invention relates to the use of fluorescent proteins, particularly
green fluorescent protein (GFP) , in fusion

random peptide library screening: laboratory techniques

L16 ANSWER 5 OF 9 BIOSIS COPYRIGHT 2 0 04 BIOLOGICAL ABSTRACTS INC. on STN
AN 2003:280434 BIOSIS
DN PREV2 003 0 02 8 0434

TI Fusions of scaffold proteins with random peptide libraries.

AU Anderson, David [Inventor, Reprint Author] ; Peelle, Beau Robert

[Inventor] ; Bogenberger, Jakob Maria [Inventor]
CS ASSIGNEE: Rigel Pharmaceuticals, Inc.
PI US 6562617 May 13, 2003

SO Official Gazette of the United States Patent and Trademark Office Patents,
(May 13 2003) Vol. 1270, No. 2. http://www.uspto.gov/web/menu/patdata.html
. e-file.

ISSN: 0098-1133 (ISSN print) .
DT Patent
LA English

ED Entered STN : 11 Jun 2 003

Last Updated on STN: 11 Jun 2 003
AB The invention relates to the use of scaffold proteins, particularly

green fluorescent protein (GFP) , in fusion

constructs with random and defined peptides and peptide libraries
, to increase the cellular expression levels, decrease the cellular
catabolism, increase the conformational stability relative to linear
peptides, and to increase the steady state concentrations of the random
peptides and random peptide library members expressed in cells
for the purpose of detecting the presence of the peptides and
screening random peptide libraries. N- terminal, C-terminal, dual
N- and C-terminal and one or more internal fusions are all contemplated.
Novel fusions utilizing self-binding peptides to create a conf ormationally
stabilized fusion domain are also contemplated.
AB The invention relates to the use of scaffold proteins, particularly
green fluorescent protein (GFP) , in fusion

ANSWER 6 OF 9 BIOSIS COPYRIGHT 2 004 BIOLOGICAL ABSTRACTS INC. on STN
2003 :227250 BIOSIS
PREV200300227250

Fusions of scaffold proteins with random peptide libraries.
Anderson, David [Inventor, Reprint Author] ; Peelle, Beau Robert
[Inventor] ; Bogenberger, Jakob Maria [Inventor]
San Bruno, CA, USA

ASSIGNEE: Rigel Pharmaceuticals, Inc.

L16

PI US 6548249 April 15, 2003

SO Official Gazette of the United States Patent and Trademark Office Patents,
(Apr 15 2003) Vol. 1269, No. 3. http://www.uspto.gov/web/menu/patdata.html
. e-file.

ISSN: 0098-1133 (ISSN print) .
DT Patent
LA English

ED Entered STN : 7 May 2 003

Last Updated on STN : 7 May 2003
AB The invention relates to the use of scaffold proteins, particularly

green fluorescent protein (GFP) , in fusion

constructs with random and defined peptides and peptide libraries
, to increase the cellular expression levels, decrease the cellular
catabolism, increase the conformational stability relative to linear
peptides, and to increase the steady state concentrations of the random
peptides and random peptide library members expressed in cells
for the purpose of detecting the presence of the peptides and
screening random peptide libraries. N-terminal, C-terminal, dual
N- and C-terminal and one or more internal fusions are all contemplated.
Novel fusions utilizing self-binding peptides to create a conf ormationally
stabilized fusion domain are also contemplated.
AB The invention relates to the use of scaffold proteins, particularly
green fluorescent protein (GFP) , in fusion

peptide detection: laboratory techniques; random peptide library

screening: laboratory techniques

L16 ANSWER 7 OF 9 CAPLUS COPYRIGHT 2004 ACS on STN
AN 2000:241464 CAPLUS
DN 132:261918

TI Fusions of scaffold proteins with random peptide libraries
IN Anderson, David; Bogenberger, Jakob Maria; Peelle, Beau Robert
PA Rigel Pharmaceuticals, Inc., USA
SO PCT Int. Appl., 89 pp.

CODEN: PIXXD2
DT Patent
LA English
FAN.CNT 4

PATENT NO. KIND DATE APPLICATION NO. DATE

2000020574

20000413

WO 1999-US23715

19991008

2000020574

20000921

AE,

AL,

AM,

AT,

AU,

AZ,

BA,

BB,

BG,

BR,

BY,

CA,

CH,

CN,

cu,

cz,

DE,

DK,

EE,

ES,

FI,

GB,

GD,

GE,

GH,

GM,

HR,

HU,

ID,

IL,

IN,

is,

JP,

KE,

KG,

KP,

KR,

KZ,

LC,

LK,

LR,

LS,

LT,

LU,

LV,

MD,

MG,

MK,

MN,

MW,

MX,

NO,

NZ,

PL,

PT,

RO,

RU,

SD,

SE,

SG,

SI,

SK,

SL,

TJ,

TM,

TR,

TT,

TZ,

UA,

UG,

UZ,

VN,

YU,

ZA,

ZW,

AM,

AZ,

BY,

KG,

KZ,

MD,

RU,

TJ,

RW:

GH,

GM,

KE,

LS,

MW,

SD,

SL,

SZ,

TZ,

UG,

ZW,

AT,

BE,

CH,

CY,

DE,

DK,

ES,

FI,

FR,

GB,

GR,

IE,

IT,

LU,

MC,

NL,

PT,

SE,

BF,

BJ,

CF,

CG,

CI,

CM,

GA,

GN,

GW,

ML,

MR,

NE,

SN,

TD,

6180343

20010130

US 1998-169015

19981008

2345215

20000413

CA 1999-2345215

19991008

1119617

20010801

EP 1999-957466

19991008

AT,

BE,

CH,

DE,

DK,

ES,

FR,

GB,

GR,

IT,

LI,

LU,

NL,

SE,

MC,

PT,

IE, SI, LT, LV, FI, RO
JP 2002526108 T2 20020820 JP 2000-574670 19991008

AU 768126 B2 20031204 AU 2000-15164 19991008

US 2001003650 Al 20010614 US 2000-749959 20001227

US 6596485 B2 20030722

PRAI US 1998-169015 A 19981008
WO 1999-US23715 W 19991008

AB The invention relates to the use of scaffold proteins, particularly
green fluorescent protein (GFP) , in fusion

constructs with random and defined peptides and peptide libraries
, to increase the cellular expression levels, decrease the cellular
catabolism, increase the conformational stability relative to linear
peptides, and to increase the steady state concns . of the random peptides
and random peptide library members expressed in cells for the
purpose of detecting the presence of the peptides and screening
random peptide libraries. N- terminal, C- terminal, dual N- and C- terminal
and one or more internal fusions are all contemplated. Novel fusions
utilizing self -binding peptides to create a conf ormationally stabilized
fusion domain are also contemplated. Thus, expts. to identify sites which
may be used to insert peptides into GFP are described.
AB The invention relates to the use of scaffold proteins, particularly
green fluorescent protein (GFP) , in fusion

constructs with random and defined peptides and peptide libraries
, to increase the cellular expression levels, decrease the cellular
catabolism, increase the conformational stability relative to linear
peptides, and to increase the steady state concns. of the random peptides
and random peptide library members expressed in cells for the
purpose of detecting the presence of the peptides and screening
random peptide libraries. N-terminal, C-terminal, dual N- and C- terminal
and one or more internal fusions are all contemplated. Novel fusions
utilizing self-binding peptides to create a conf ormationally stabilized
fusion domain are also contemplated. Thus, expts. to identify sites which
may be used to insert peptides into GFP are described.
ST scaffold protein peptide fusion library; green fluorescent
protein peptide fusion library

LI 6 ANSWER 8 OF 9 CAPLUS COPYRIGHT 2 0 04 ACS on STN
AN 2000:114405 CAPLUS
DN 132:147593

TI Methods and compositions for peptide libraries displayed on light-emitting

scaffolds of proteins
IN Kamb, Carl Alexander; Abedi , Ma j id
PA Arcaris, Inc., USA

SO U.S., 24 pp., Cont. -in-part of U.S. 5,955,275.

CODEN: USXXAM
DT Patent
LA English
FAN.CNT 11

PATENT NO. KIND DATE APPLICATION NO. DATE

6025485

20000215

6623922

20030923

5955275

19990921

2309543

19990520

9924617

19990520

AL,

AM,

AT, AU,

AZ,

BA,

BB,

DK,

EE,

ES, FI,

GB,

GD,

GE,

KG,

KP,

KR, KZ,

LC,

LK,

LR,

MX,

NO,

NZ, PL,

PT,

RO,

RU,

TT,

UA,

UG, US,

UZ,

VN,

YU,

RW:

GH,

GM,

KE, LS,

MW,

SD,

SZ,

FI,

FR,

GB, GR,

IE,

IT,

LU,

CM,

GA,

GN, GW,

ML,

MR,

NE,

9915200

19990531

US 1997-965477 19971106

US 1997-800664 19970214

US 1997-812994 19970304

CA 1998-2309543 19981106

WO 1998-US23778 19981106

BG,

BR,

BY,

CA,

CH,

CN,

CU,

CZ,

DE,

GH,

GM,

HR,

HU,

ID,

IL,

IS,

JP,

KE,

LS,

LT,

LU,

LV,

MD,

MG,

MK,

MN,

MW,

SD,

SE,

SG,

SI /

SK,

SL,

TJ,

TM,

TR,

ZW,

AM,

AZ,

BY,

KG,

KZ,

MD,

RU,

TJ,

UG,

ZW,

AT,

BE,

CH,

CY,

DE,

DK,

ES,

MC,

NL,

PT,

SE,

BF,

BJ,

CF,

CG,

CI,

SN,

TD,

AU 1999-15200 19981106

EP 1029081 Al 20000823 EP 1998-959391 19981106

R: AT, BE, CH, DE, DK, ES, FR, GB, GR, IT, LI, LU, NL, SE, MC, PT,

IE, FI

o /\ /*k i r~ «™» i r - n

2 001522587

2 001112 0

2000 -

519609

T QQ01 1 A C

iy y oi iuo

6566057

2003 052 0

1999-

269006

iy y yuj l /

2 000002375

2000063 0

2000-

2375

zUUUUoUb

2 00213222 9

2002 0919

2001-

929663

2. U U 10 o 14

2002090605

2002 0711

2001-

935929

20010823

PRAI US

1997-800664

19970214

1997-812994

19970304

1996-699266

19960819

1997-US14514

19970819

1997-965477

19971106

1998-US23778

19981106

1999-259155

19990226

1999-378420

19990820

AB Methods and compns . for peptides or protein fragments displayed on
scaffolds and libraries of sequences encoding peptides or protein
fragments displayed on scaffolds that permit the properties of the library
to be easily and quant, monitored are disclosed. The scaffold is a
protein that is capable of emitting light. Thus, solvent -exposed loops
are identified in the Aequorea victoria green fluorescent protein (GFP)
which can accommodate and present random aptamers while allowing GFP to
retain its autof luorescent properties; these loops optimally comprise
amino acid residues Alal55 -Ilel61, Lysl62-Glnl83 , and Glnl84 -Ser205 . A
minibody (Ig) -GFP scaffold system is also described. The plasmid vector
pVT21, which permits induction of GFP expression in the presence of
galactose, was obtained by manipulation of pACA151, a 6.7-kb 2\jl yeast
shuttle vector containing a red-shifted (S65T) GFP expression cassette and the
phosphoglycerate kinase 3" end. Thus, anal, of the expression of
individual members of the library when they are expressed in
cells may be carried out using instruments that can analyze the emitted
light, such as flow sorter (FACS) , a spectrophotometer, a microtiter plate
reader, a CCD, a fluorescence microscope, or other similar device. This
permits screening of the expression library in host cells on a
cell -by-cell basis, and enrichment of the library for sequences that have
predetd . characteristics .

RE.CNT 7 THERE ARE 7 CITED REFERENCES AVAILABLE FOR THIS RECORD

ALL CITATIONS AVAILABLE IN THE RE FORMAT

AB Methods and compns. for peptides or protein fragments displayed on
scaffolds and libraries of sequences encoding peptides or protein
fragments displayed on scaffolds that permit the properties of the library
to be easily and quant, monitored are disclosed. The scaffold is a
protein that is capable of emitting light. Thus, solvent -exposed loops
are identified in the Aequorea victoria green fluorescent protein (GFP)
which can accommodate and present random aptamers while allowing GFP to
retain its autof luorescent properties; these loops optimally comprise
amino acid residues Alal55 -Ilel61, Lysl62 -Glnl83 , and Glnl84 -Ser205 . A
minibody (Ig) -GFP scaffold system is also described. The plasmid vector
pVT21, which permits induction of GFP expression in the presence of
galactose, was obtained by manipulation of pACA151, a 6.7-kb 2u yeast
shuttle vector containing a red-shifted (S65T) GFP expression cassette and the
phosphoglycerate kinase 3' end. Thus, anal, of the expression of
individual members of the library when they are expressed in
cells may be carried out using instruments that can analyze the emitted
light, such as flow sorter (FACS) , a spectrophotometer, a microtiter plate
reader, a CCD, a fluorescence microscope, or other similar device. This
permits screening of the expression library in host cells on a
cell -by-cell basis, and enrichment of the library for sequences that have
predetd. characteristics.

IT Immunoglobulins

RL: ARU (Analytical role, unclassified); BPN (Biosynthetic preparation);
BPR (Biological process) ,- BSU (Biological study, unclassified) ; ANST
(Analytical study) ; BIOL (Biological study) ; PREP (Preparation) ; PROC

(Process)

(fusion products, green fluorescent protein

fusion library; methods and compns . for peptide

libraries displayed on light -emitting scaffolds of proteins)

L16 ANSWER 9 OF 9 CAPLUS COPYRIGHT 2 004 ACS on STM
AN 1999:330461 CAPLUS
DN 130:333721

TI Methods and compositions for peptide libraries displayed on light-emitting

scaffolds of proteins
IN Kamb, Carl Alexander; Abedi, Majid
PA Ventana Genetics, Inc., USA
SO PCT Int. Appl., 56 pp.

CODEN: PIXXD2
DT Patent
LA English

FAN.CNT 11

PATENT NO.

KIND

DATE

APPLICATION NO.

DATE

PI WO

'9924617

19990520

WO 1998-US23778

19981106

W: AL,

AM,

AT, AU,

AZ,

BA,

BB,

BG, BR,

BY,

CA, CH,

CN, CU,

CZ,

DE,

DK,

EE,

ES, FI,

GB,

GD,

GE,

GH, GM,

HR,

HU, ID,

IL, IS,

UP/

KE,

KG,

KP,

KR, KZ,

LC,

LK,

LR,

LS, LT,

LU,

LV, MD,

MG, MK,

MN,

MW,

MX,

NO,

NZ , PL ,

PT,

RO,

RU,

SD, SE,

SG,

SI, SK,

SL, TJ,

TM,

TR,

TT,

UA,

UG, US,

UZ,

VN,

YU,

ZW, AM,

AZ,

BY, KG,

KZ, MD,

RU,

TJ,

RW: GH,

GM,

KE, LS,

MW,

SD,

SZ,

UG, ZW,

AT,

BE, CH,

CY, DE,

DK,

ES,

FI,

FR,

GB, GR,

IE,

IT,

LU,

MC, NL,

PT,

SE, BF,

BJ, CF,

CG,

CI,

CM,

GA,

GN, GW,

ML,

MR,

NE,

SN, TD,

6025485

20000215

US 1997-965477

19971106

2309543

19990520

CA 1998-2309543

19981106

9915200

19990531

AU 1999-15200

19981106

1029081

20000823

EP 1998-959391

19981106

R: AT,

BE,

CH, DE,

DK,

ES,

FR,

GB, GR,

IT,

LI, LU,

NL, SE,

MC,

PT,

IE,

2001522587

20011120

JP 2000-519609

19981106

6566057

20030520

US 1999-269006

19990317

2000002375

20000630

NO 2000-2375

20000505

PRAI US

1997-965477

19971106

1997-800664

19970214

1997-812994

19970304

1998-US23778

19981106

RE.CNT 4 THERE ARE 4 CITED REFERENCES AVAILABLE FOR THIS RECORD

ALL CITATIONS AVAILABLE IN THE RE FORMAT

This permits screening of the expression library in host cells

on a cell -by-cell basis, and enrichment of the library for sequences that

have predetd. characteristics.
ST peptide library fusion light emitting scaffold

green fluorescent protein
IT Immunoglobulins

RL: ARU (Analytical role, unclassified) ; BPN (Biosynthetic preparation) ;

BPR (Biological process) ; BSU (Biological study, unclassified) ; ANST

(Analytical study) ; BIOL (Biological study) ; PREP (Preparation) ; PROC

(Process)

(green fluorescent protein fusion

library; methods and compns . for peptide libraries
displayed on light-emitting scaffolds of proteins)

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